Evidence map›Paper›PMID 28029251›Full record

ArticleJournal of the American Chemical Society2017

Diversity of Secondary Structure in Catalytic Peptides with β-Turn-Biased Sequences.

Anthony J Metrano, Nadia C Abascal, Brandon Q Mercado, Eric K Paulson, Anna E Hurtley, Scott J Miller

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
7.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 129 citations in OpenAlex.

  1. Total Synthesis of Xentrivalpeptide A and Its 6α-Molecules (Basel, Switzerland) · 2026
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  4. Desymmetrization ofJournal of the American Chemical Society · 2026
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  20. Aspartyl β-Turn-Based Dirhodium(II) Metallopeptides for Benzylic C(spJournal of the American Chemical Society · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Anthony J MetranoDepartment of Chemistry, Yale University , P.O. Box 208107, New Haven, Connecticut 06520-8107, United States.
Nadia C AbascalDepartment of Chemistry, Yale University , P.O. Box 208107, New Haven, Connecticut 06520-8107, United States.
Brandon Q MercadoDepartment of Chemistry, Yale University , P.O. Box 208107, New Haven, Connecticut 06520-8107, United States.
Eric K PaulsonDepartment of Chemistry, Yale University , P.O. Box 208107, New Haven, Connecticut 06520-8107, United States.
Anna E HurtleyDepartment of Chemistry, Yale University , P.O. Box 208107, New Haven, Connecticut 06520-8107, United States.
Scott J MillerDepartment of Chemistry, Yale University , P.O. Box 208107, New Haven, Connecticut 06520-8107, United States.ORCID 0000-0001-7817-1318
Yale University · US

Funding

Site-Selective Catalysis for Organic SynthesisR37GM068649 · NIGMS · YALE UNIVERSITY · PI MILLER, SCOTT J · 2011 to 2018
$2.7M
Selective Peptide-Based Oxidation Catalysts for Bioactive Molecule SynthesisR01GM096403 · NIGMS · YALE UNIVERSITY · PI MILLER, SCOTT J · 2011 to 2018
$2.4M
Site-Selective Catalysts for Organic SynthesisR01GM068649 · NIGMS · YALE UNIVERSITY · PI MILLER, SCOTT J · 2003 to 2010
$2.3M
NIGMS NIH HHS R01 GM068649NIGMS NIH HHS R01 GM096403NIGMS NIH HHS R37 GM068649
6 · The paper itself

Abstract

X-ray crystallography has been applied to the structural analysis of a series of tetrapeptides that were previously assessed for catalytic activity in an atroposelective bromination reaction. Common to the series is a central Pro-Xaa sequence, where Pro is either l- or d-proline, which was chosen to favor nucleation of canonical β-turn secondary structures. Crystallographic analysis of 35 different peptide sequences revealed a range of conformational states. The observed differences appear not only in cases where the Pro-Xaa loop-region is altered, but also when seemingly subtle alterations to the flanking residues are introduced. In many instances, distinct conformers of the same sequence were observed, either as symmetry-independent molecules within the same unit cell or as polymorphs. Computational studies using DFT provided additional insight into the analysis of solid-state structural features. Select X-ray crystal structures were compared to the corresponding solution structures derived from measured proton chemical shifts,

Indexed as

CatalysisCrystallography, X-RayModels, MolecularPeptidesProtein ConformationQuantum TheoryPeptides

Identifiers

PMID28029251
PMCPMC5312972
OpenAlexW2562417815

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.